ID S0DIR1_GIBF5 Unreviewed; 1092 AA.
AC S0DIR1;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU367027};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU367027};
GN ORFNames=FFUJ_01064 {ECO:0000313|EMBL:CCT62389.1};
OS Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS and foot rot disease fungus) (Fusarium fujikuroi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=1279085 {ECO:0000313|EMBL:CCT62389.1, ECO:0000313|Proteomes:UP000016800};
RN [1] {ECO:0000313|Proteomes:UP000016800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831
RC {ECO:0000313|Proteomes:UP000016800};
RX PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA Wiemann P., Sieber C.M., von Bargen K.W., Studt L., Niehaus E.M.,
RA Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA Proctor R.H., Munsterkotter M., Freitag M., Humpf H.U., Guldener U.,
RA Tudzynski B.;
RT "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT novel metabolites.";
RL PLoS Pathog. 9:E1003475-E1003475(2013).
CC -!- FUNCTION: ATP-dependent DNA helicase involved in DNA damage repair by
CC homologous recombination and in genome maintenance. Capable of
CC unwinding D-loops. Plays a role in limiting crossover recombinants
CC during mitotic DNA double-strand break (DSB) repair. Component of a
CC FANCM-MHF complex which promotes gene conversion at blocked replication
CC forks, probably by reversal of the stalled fork.
CC {ECO:0000256|ARBA:ARBA00003813, ECO:0000256|RuleBase:RU367027}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665,
CC ECO:0000256|RuleBase:RU367027};
CC -!- SUBUNIT: Interacts with the MHF histone-fold complex to form the FANCM-
CC MHF complex. {ECO:0000256|ARBA:ARBA00011390,
CC ECO:0000256|RuleBase:RU367027}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU367027}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC FANCM sub-subfamily. {ECO:0000256|ARBA:ARBA00009889,
CC ECO:0000256|RuleBase:RU367027}.
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DR EMBL; HF679023; CCT62389.1; -; Genomic_DNA.
DR AlphaFoldDB; S0DIR1; -.
DR STRING; 1279085.S0DIR1; -.
DR EnsemblFungi; CCT62389; CCT62389; FFUJ_01064.
DR VEuPathDB; FungiDB:FFUJ_01064; -.
DR HOGENOM; CLU_002513_0_1_1; -.
DR OrthoDB; 12149at2759; -.
DR Proteomes; UP000016800; Chromosome 1.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR CDD; cd18033; DEXDc_FANCM; 1.
DR CDD; cd12091; FANCM_ID; 1.
DR CDD; cd18801; SF2_C_FANCM_Hef; 1.
DR Gene3D; 1.20.1320.20; hef helicase domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR039686; FANCM/Mph1-like_ID.
DR InterPro; IPR044749; FANCM_DEXDc.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR14025; FANCONI ANEMIA GROUP M FANCM FAMILY MEMBER; 1.
DR PANTHER; PTHR14025:SF20; FANCONI ANEMIA GROUP M PROTEIN; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF04851; ResIII; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:CCT62389.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000016800}.
FT DOMAIN 162..330
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 506..666
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 22..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..1051
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..934
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..959
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..988
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1028
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1092 AA; 121744 MW; 157165F2F366DCA4 CRC64;
MDSDEFDDDI ADEDFITALD QVSSSMNGQG NTKPSHAVVS RPSNKPNSAA VAALELEDLP
SDAFSSPEPQ SRSNVSVAAS AGPAPRTGLN RTSSGNWRQT TLFGGSLSSD GPHTSQPAAA
TRVFRADLPR EEPTHHEVDT EAMQTWVYPT NLGAIRNYQF SIVKNSLFNN TLVALPTGLG
KTFIAATVML NFYRWTKKAK LVFVAPTKPL VAQQVDACYN IAGIPRSETT LLTGDIPPAL
RVDEWESRRV FFMTPQTLLN DISHGYADPK SIALLVIDEA HRAVGEYAYA KVTKLIRRFS
KSFRVLALTA TPGSKIETVQ EVIDNLGISH CEIRTEDSID IRQYVHQRNI EQVVLDPSDE
MILVSELFTK ALKPMTDKLS SQNIWFGRSP MAITAYGLMQ SQREWFASRG RHANQGVQHM
MRAVFSVLTS IAHSIKLLNF HGIKPFYDNL VDLRSEQEGK GEKGSKYKRQ LIQDSNFQEM
MDKISKWLRT EGFVGHPKLT ALADTVLNHF MDQSENSATR VIVFSEYRDS AEDIVRMLNK
HQPLIKASVF VGQADGKRGE GMKQAQQIEA INRFKRGDFN VLVATSIGEE GLDIGQVDLI
VCYDSSASPI RMLQRMGRTG RKRAGNIVLL LMRGKEEDQF AKSKDNYEKM QTLICEGSRF
NFRFDLSTRI VPRGVVPEVD KRHVDIPIEN TQDQSLPEPK KRRAPAGKKK PPKKFHMPDG
VETGFQSVAS LLKIGGKAKQ QSNKHNPELG DLATLPELSK VLLDDEELKE LNRAYRNLPF
NHSIIEETDM PDMTAHPELQ RQLRPVFKLK HGIRTKRFVK LWHKMAHDPE SLVLPCRYQD
RSNYLEIPVH AFAGSGSETE PADETPTTKA KGMGAKAPVT KKQNRKPPSK AQPRAKRRRL
SSDLAPQTFA VGSMVDEGLF EEDDEDDDED EEDEVIPRGR GRPKRSSKSG SKGKRRPRQK
QGGLNSDEVG DDCERDSDMI ETDGSDNGED LLDFIVSDNH PMSSGREPVS LRTSSPPASS
TSTPECAHGK STKPFYVPTQ FPGTQESDDI PDLGEVLKMT GKQRAQDFSD DDVAVRRTAR
GRRAVVDESD SD
//
